Chlorine in PDB 5aa2: Crystal Structure of Mltf From Pseudomonas Aeruginosa in Complex with Nam-Pentapeptide.

The structure of Crystal Structure of Mltf From Pseudomonas Aeruginosa in Complex with Nam-Pentapeptide., PDB code: 5aa2 was solved by T.Dominguez-Gil, I.Acebron, J.A.Hermoso, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.26 / 2.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	65.585, 135.652, 137.459, 90.00, 92.06, 90.00
R / Rfree (%)	16.7 / 23.5

The binding sites of Chlorine atom in the Crystal Structure of Mltf From Pseudomonas Aeruginosa in Complex with Nam-Pentapeptide. (pdb code 5aa2). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Mltf From Pseudomonas Aeruginosa in Complex with Nam-Pentapeptide., PDB code: 5aa2:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Mltf From Pseudomonas Aeruginosa in Complex with Nam-Pentapeptide.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Mltf From Pseudomonas Aeruginosa in Complex with Nam-Pentapeptide. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1446 b:61.2 occ:1.00 OG A:SER366 3.9 30.2 1.0 OH A:TYR437 4.1 46.7 1.0 CB A:SER366 4.3 33.8 1.0 OE1 A:GLU362 4.3 47.5 1.0 CE2 A:TYR437 4.4 38.6 1.0 CH2 A:TRP367 4.5 37.0 1.0 CZ A:TYR437 4.7 40.9 1.0 CD2 A:LEU295 4.8 24.5 1.0 CZ3 A:TRP367 4.9 30.0 1.0 CB A:PRO363 5.0 37.8 1.0 CZ2 A:TRP367 5.0 40.5 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Mltf From Pseudomonas Aeruginosa in Complex with Nam-Pentapeptide.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Mltf From Pseudomonas Aeruginosa in Complex with Nam-Pentapeptide. within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl1446 b:0.5 occ:1.00 NH2 C:ARG47 3.4 61.3 1.0 CE2 C:TYR348 3.8 65.0 1.0 O C:MET321 3.9 71.1 1.0 NE C:ARG47 4.0 52.9 1.0 OG1 C:THR326 4.1 77.0 1.0 CZ C:ARG47 4.1 64.5 1.0 CD2 C:TYR348 4.1 68.0 1.0 CA C:LEU322 4.3 56.7 1.0 N C:THR323 4.4 64.8 1.0 O C:TYR373 4.5 49.0 1.0 CG2 C:THR323 4.5 70.7 1.0 CD2 C:LEU322 4.5 65.5 1.0 CZ C:TYR373 4.5 51.1 1.0 CB C:THR326 4.5 63.3 1.0 CE1 C:TYR373 4.5 42.3 1.0 CG2 C:THR326 4.6 58.0 1.0 OH C:TYR373 4.6 59.1 1.0 CZ C:TYR348 4.8 61.8 1.0 C C:MET321 4.8 66.2 1.0 C C:LEU322 4.8 63.0 1.0 CE2 C:TYR373 5.0 44.7 1.0

T.Dominguez-Gil, M.Lee, I.Acebron-Avalos, K.V.Mahasenan, D.Hesek, D.A.Dik, B.Byun, E.Lastochkin, J.F.Fisher, S.Mobashery, J.A.Hermoso. Activation By Allostery in Cell-Wall Remodeling By A Modular Membrane-Bound Lytic Transglycosylase From Pseudomonas Aeruginosa. Structure V. 24 1729 2016.
ISSN: ISSN 1878-4186
PubMed: 27618662
DOI: 10.1016/J.STR.2016.07.019